enterococcal standard strains Search Results


99
ATCC standard laboratory e faecalis strains
Strains used in this study.
Standard Laboratory E Faecalis Strains, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Zymo Research fungal strains
Strains used in this study.
Fungal Strains, supplied by Zymo Research, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC enterococcus faecalis strain
Mean values of surface area (μ 2 ) of E. <t>faecalis</t> biofilm on the canal surface at 3, 2, and 1 mm from the canal terminus, before and after irrigation protocols. The black arrow on the y ‐axis indicates breaks of different value axis scaling. Error bars are standard deviation ( n = 3 per group)
Enterococcus Faecalis Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
ATCC enterococcus hirae atcc 10541
Mean values of surface area (μ 2 ) of E. <t>faecalis</t> biofilm on the canal surface at 3, 2, and 1 mm from the canal terminus, before and after irrigation protocols. The black arrow on the y ‐axis indicates breaks of different value axis scaling. Error bars are standard deviation ( n = 3 per group)
Enterococcus Hirae Atcc 10541, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC standard strain atcc 33186
Mean values of surface area (μ 2 ) of E. <t>faecalis</t> biofilm on the canal surface at 3, 2, and 1 mm from the canal terminus, before and after irrigation protocols. The black arrow on the y ‐axis indicates breaks of different value axis scaling. Error bars are standard deviation ( n = 3 per group)
Standard Strain Atcc 33186, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC standard strains
Mean values of surface area (μ 2 ) of E. <t>faecalis</t> biofilm on the canal surface at 3, 2, and 1 mm from the canal terminus, before and after irrigation protocols. The black arrow on the y ‐axis indicates breaks of different value axis scaling. Error bars are standard deviation ( n = 3 per group)
Standard Strains, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC standard reference strains
Mean values of surface area (μ 2 ) of E. <t>faecalis</t> biofilm on the canal surface at 3, 2, and 1 mm from the canal terminus, before and after irrigation protocols. The black arrow on the y ‐axis indicates breaks of different value axis scaling. Error bars are standard deviation ( n = 3 per group)
Standard Reference Strains, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC standard reference bacterial strains
Mean values of surface area (μ 2 ) of E. <t>faecalis</t> biofilm on the canal surface at 3, 2, and 1 mm from the canal terminus, before and after irrigation protocols. The black arrow on the y ‐axis indicates breaks of different value axis scaling. Error bars are standard deviation ( n = 3 per group)
Standard Reference Bacterial Strains, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
ATCC e faecium
The cell adhesion ability and maximal protein binding capacity of LAB. A monolayer of Int 407 cells (10 4 /well) were mixed without LAB (sample 1), or with 1 × 10 7 CFU of E. <t>faecium</t> (standard strain ATCC 6057) (sample 2), E. faecium 63b-2 (sample 3), or E. faecium 58a-1 (sample 4). After 2 h, the cells were thoroughly washed and fixed with 10% formaldehyde, followed by Gram staining (A). The maximum binding capacity of the AcmA′ fusion protein to LAB was determined as follows. Various concentrations of AcmA′-GFP fusion protein (0, 5, 10, 20, and 50 μg indicated as sample 1–5, respectively) were mixed with 1 × 10 9 CFU of E. faecium 63b-2 at 30 °C for 3 h followed by intensive washes with PBS. After centrifugation, the supernatant containing unbound AcmA-GFP fusion protein was transferred to a new tube and the pellet containing the LAB anchored GFP fusion protein was directly examined by fluorescent microscopy (B). In addition, to evaluate the binding efficiency, the anchored form (C) and free form (D) of GFP fusion proteins were then analyzed with SDS-PAGE. Binding efficiency was determined by the ratio of AcmA′ fusion protein present in the bacteria pellet (anchored form) (C) to that in supernatant (free form) (D).
E Faecium, supplied by ATCC, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC bacterial strains
The cell adhesion ability and maximal protein binding capacity of LAB. A monolayer of Int 407 cells (10 4 /well) were mixed without LAB (sample 1), or with 1 × 10 7 CFU of E. <t>faecium</t> (standard strain ATCC 6057) (sample 2), E. faecium 63b-2 (sample 3), or E. faecium 58a-1 (sample 4). After 2 h, the cells were thoroughly washed and fixed with 10% formaldehyde, followed by Gram staining (A). The maximum binding capacity of the AcmA′ fusion protein to LAB was determined as follows. Various concentrations of AcmA′-GFP fusion protein (0, 5, 10, 20, and 50 μg indicated as sample 1–5, respectively) were mixed with 1 × 10 9 CFU of E. faecium 63b-2 at 30 °C for 3 h followed by intensive washes with PBS. After centrifugation, the supernatant containing unbound AcmA-GFP fusion protein was transferred to a new tube and the pellet containing the LAB anchored GFP fusion protein was directly examined by fluorescent microscopy (B). In addition, to evaluate the binding efficiency, the anchored form (C) and free form (D) of GFP fusion proteins were then analyzed with SDS-PAGE. Binding efficiency was determined by the ratio of AcmA′ fusion protein present in the bacteria pellet (anchored form) (C) to that in supernatant (free form) (D).
Bacterial Strains, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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99
ATCC enterococcus faecalis
The cell adhesion ability and maximal protein binding capacity of LAB. A monolayer of Int 407 cells (10 4 /well) were mixed without LAB (sample 1), or with 1 × 10 7 CFU of E. <t>faecium</t> (standard strain ATCC 6057) (sample 2), E. faecium 63b-2 (sample 3), or E. faecium 58a-1 (sample 4). After 2 h, the cells were thoroughly washed and fixed with 10% formaldehyde, followed by Gram staining (A). The maximum binding capacity of the AcmA′ fusion protein to LAB was determined as follows. Various concentrations of AcmA′-GFP fusion protein (0, 5, 10, 20, and 50 μg indicated as sample 1–5, respectively) were mixed with 1 × 10 9 CFU of E. faecium 63b-2 at 30 °C for 3 h followed by intensive washes with PBS. After centrifugation, the supernatant containing unbound AcmA-GFP fusion protein was transferred to a new tube and the pellet containing the LAB anchored GFP fusion protein was directly examined by fluorescent microscopy (B). In addition, to evaluate the binding efficiency, the anchored form (C) and free form (D) of GFP fusion proteins were then analyzed with SDS-PAGE. Binding efficiency was determined by the ratio of AcmA′ fusion protein present in the bacteria pellet (anchored form) (C) to that in supernatant (free form) (D).
Enterococcus Faecalis, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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95
ATCC faecalis standard strain
The cell adhesion ability and maximal protein binding capacity of LAB. A monolayer of Int 407 cells (10 4 /well) were mixed without LAB (sample 1), or with 1 × 10 7 CFU of E. <t>faecium</t> (standard strain ATCC 6057) (sample 2), E. faecium 63b-2 (sample 3), or E. faecium 58a-1 (sample 4). After 2 h, the cells were thoroughly washed and fixed with 10% formaldehyde, followed by Gram staining (A). The maximum binding capacity of the AcmA′ fusion protein to LAB was determined as follows. Various concentrations of AcmA′-GFP fusion protein (0, 5, 10, 20, and 50 μg indicated as sample 1–5, respectively) were mixed with 1 × 10 9 CFU of E. faecium 63b-2 at 30 °C for 3 h followed by intensive washes with PBS. After centrifugation, the supernatant containing unbound AcmA-GFP fusion protein was transferred to a new tube and the pellet containing the LAB anchored GFP fusion protein was directly examined by fluorescent microscopy (B). In addition, to evaluate the binding efficiency, the anchored form (C) and free form (D) of GFP fusion proteins were then analyzed with SDS-PAGE. Binding efficiency was determined by the ratio of AcmA′ fusion protein present in the bacteria pellet (anchored form) (C) to that in supernatant (free form) (D).
Faecalis Standard Strain, supplied by ATCC, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Strains used in this study.

Journal: Journal of Oral Microbiology

Article Title: The potential regulatory role of mannose phosphotransferase system EII in alkaline resistance of Enterococcus faecalis

doi: 10.1080/20002297.2025.2487944

Figure Lengend Snippet: Strains used in this study.

Article Snippet: We compared the alkaline resistance of these six strains, along with two standard laboratory E. faecalis strains (ATCC 29212 and ATCC 51299), through alkaline resistance analysis.

Techniques: Preserving, Over Expression

Biological characteristics, growth kinetic assay and morphology of E. faecalis at pH 7 and 10. (a) Bacterial suspensions of ATCC 29212, Δ mptD and + mptD . (b, c) crystal violet staining biofilms and biofilm mass analysis of ATCC 29212, Δ mptD and + mptD . (d) Cell morphologies of ATCC 29212, Δ mptD and + mptD at exponential growth phase (10,000×). (e) Growth kinetics of ATCC 29212, Δ mptD and + mptD for 24 h. * p < 0.05; *** p < 0.001; **** p < 0.0001.

Journal: Journal of Oral Microbiology

Article Title: The potential regulatory role of mannose phosphotransferase system EII in alkaline resistance of Enterococcus faecalis

doi: 10.1080/20002297.2025.2487944

Figure Lengend Snippet: Biological characteristics, growth kinetic assay and morphology of E. faecalis at pH 7 and 10. (a) Bacterial suspensions of ATCC 29212, Δ mptD and + mptD . (b, c) crystal violet staining biofilms and biofilm mass analysis of ATCC 29212, Δ mptD and + mptD . (d) Cell morphologies of ATCC 29212, Δ mptD and + mptD at exponential growth phase (10,000×). (e) Growth kinetics of ATCC 29212, Δ mptD and + mptD for 24 h. * p < 0.05; *** p < 0.001; **** p < 0.0001.

Article Snippet: We compared the alkaline resistance of these six strains, along with two standard laboratory E. faecalis strains (ATCC 29212 and ATCC 51299), through alkaline resistance analysis.

Techniques: Kinetic Assay, Staining

The membrane potential of E. faecalis at pH 7 and 10. (a) Flow cytometry dot plots showing membrane potential of ATCC 29212, Δ mptD and + mptD , gates indicate the proportion of the hyperpolarized cell population. (b, c) membrane potential and permeability of ATCC 29212, Δ mptD and + mptD . **** p < 0.0001.

Journal: Journal of Oral Microbiology

Article Title: The potential regulatory role of mannose phosphotransferase system EII in alkaline resistance of Enterococcus faecalis

doi: 10.1080/20002297.2025.2487944

Figure Lengend Snippet: The membrane potential of E. faecalis at pH 7 and 10. (a) Flow cytometry dot plots showing membrane potential of ATCC 29212, Δ mptD and + mptD , gates indicate the proportion of the hyperpolarized cell population. (b, c) membrane potential and permeability of ATCC 29212, Δ mptD and + mptD . **** p < 0.0001.

Article Snippet: We compared the alkaline resistance of these six strains, along with two standard laboratory E. faecalis strains (ATCC 29212 and ATCC 51299), through alkaline resistance analysis.

Techniques: Membrane, Flow Cytometry, Permeability

The intracellular potassium ions concentration and pH, as well as cellular energy metabolism of E. faecalis at pH 7 and 10. (a) Intracellular potassium ion (K + ) concentration of ATCC 29212, Δ mptD and + mptD are indicated by fluorescence intensity (green). (b) Quantification of intracellular K + concentration of ATCC 29212, Δ mptD and + mptD . (c) Intracellular pH (pH in ) of ATCC 29212, Δ mptD and + mptD . (d) Cellular ATP concentration of ATCC 29212, Δ mptD and + mptD . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001.

Journal: Journal of Oral Microbiology

Article Title: The potential regulatory role of mannose phosphotransferase system EII in alkaline resistance of Enterococcus faecalis

doi: 10.1080/20002297.2025.2487944

Figure Lengend Snippet: The intracellular potassium ions concentration and pH, as well as cellular energy metabolism of E. faecalis at pH 7 and 10. (a) Intracellular potassium ion (K + ) concentration of ATCC 29212, Δ mptD and + mptD are indicated by fluorescence intensity (green). (b) Quantification of intracellular K + concentration of ATCC 29212, Δ mptD and + mptD . (c) Intracellular pH (pH in ) of ATCC 29212, Δ mptD and + mptD . (d) Cellular ATP concentration of ATCC 29212, Δ mptD and + mptD . * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001.

Article Snippet: We compared the alkaline resistance of these six strains, along with two standard laboratory E. faecalis strains (ATCC 29212 and ATCC 51299), through alkaline resistance analysis.

Techniques: Concentration Assay, Fluorescence

The alkaline resistance evaluation of E. faecalis . (a) Dynamic growth curves of E. faecalis at pH 7 and 10. (b) Representative images of CFUs and CFUs-counting comparison among groups after incubation at pH 10 for 24 h. **** p < 0.0001.

Journal: Journal of Oral Microbiology

Article Title: The potential regulatory role of mannose phosphotransferase system EII in alkaline resistance of Enterococcus faecalis

doi: 10.1080/20002297.2025.2487944

Figure Lengend Snippet: The alkaline resistance evaluation of E. faecalis . (a) Dynamic growth curves of E. faecalis at pH 7 and 10. (b) Representative images of CFUs and CFUs-counting comparison among groups after incubation at pH 10 for 24 h. **** p < 0.0001.

Article Snippet: We compared the alkaline resistance of these six strains, along with two standard laboratory E. faecalis strains (ATCC 29212 and ATCC 51299), through alkaline resistance analysis.

Techniques: Comparison, Incubation

The number of differentially expressed genes of E.  faecalis  with different  alkaline  resistance under  alkaline  condition.

Journal: Journal of Oral Microbiology

Article Title: The potential regulatory role of mannose phosphotransferase system EII in alkaline resistance of Enterococcus faecalis

doi: 10.1080/20002297.2025.2487944

Figure Lengend Snippet: The number of differentially expressed genes of E. faecalis with different alkaline resistance under alkaline condition.

Article Snippet: We compared the alkaline resistance of these six strains, along with two standard laboratory E. faecalis strains (ATCC 29212 and ATCC 51299), through alkaline resistance analysis.

Techniques: Control, Modification, Transduction

Alkaline resistance of E. faecalis positively correlated with the expression of Man-PTS EII, membrane transport and amino acid metabolism genes. (a) KEGG enrichment analysis of upregulated or downregulated DEGs. (b) Selected differential expression genes involved in Man-PTS EII and membrane transport and amino acid metabolism. (c) Comparison of mRNA expression levels of Man-PTS EII at pH 10 by RT-qPCR in E. faecalis compared to pH 7. *** p < 0.001; ** p < 0.01.

Journal: Journal of Oral Microbiology

Article Title: The potential regulatory role of mannose phosphotransferase system EII in alkaline resistance of Enterococcus faecalis

doi: 10.1080/20002297.2025.2487944

Figure Lengend Snippet: Alkaline resistance of E. faecalis positively correlated with the expression of Man-PTS EII, membrane transport and amino acid metabolism genes. (a) KEGG enrichment analysis of upregulated or downregulated DEGs. (b) Selected differential expression genes involved in Man-PTS EII and membrane transport and amino acid metabolism. (c) Comparison of mRNA expression levels of Man-PTS EII at pH 10 by RT-qPCR in E. faecalis compared to pH 7. *** p < 0.001; ** p < 0.01.

Article Snippet: We compared the alkaline resistance of these six strains, along with two standard laboratory E. faecalis strains (ATCC 29212 and ATCC 51299), through alkaline resistance analysis.

Techniques: Expressing, Membrane, Quantitative Proteomics, Comparison, Quantitative RT-PCR

Illustration of potential role of Man-PTS EII in the alkaline resistance of E. faecalis .

Journal: Journal of Oral Microbiology

Article Title: The potential regulatory role of mannose phosphotransferase system EII in alkaline resistance of Enterococcus faecalis

doi: 10.1080/20002297.2025.2487944

Figure Lengend Snippet: Illustration of potential role of Man-PTS EII in the alkaline resistance of E. faecalis .

Article Snippet: We compared the alkaline resistance of these six strains, along with two standard laboratory E. faecalis strains (ATCC 29212 and ATCC 51299), through alkaline resistance analysis.

Techniques:

Mean values of surface area (μ 2 ) of E. faecalis biofilm on the canal surface at 3, 2, and 1 mm from the canal terminus, before and after irrigation protocols. The black arrow on the y ‐axis indicates breaks of different value axis scaling. Error bars are standard deviation ( n = 3 per group)

Journal: MicrobiologyOpen

Article Title: Confocal laser scanning, scanning electron, and transmission electron microscopy investigation of Enterococcus faecalis biofilm degradation using passive and active sodium hypochlorite irrigation within a simulated root canal model

doi: 10.1002/mbo3.455

Figure Lengend Snippet: Mean values of surface area (μ 2 ) of E. faecalis biofilm on the canal surface at 3, 2, and 1 mm from the canal terminus, before and after irrigation protocols. The black arrow on the y ‐axis indicates breaks of different value axis scaling. Error bars are standard deviation ( n = 3 per group)

Article Snippet: Biofilms were grown from Enterococcus faecalis strain ( ATCC 19433), which was plated onto a BHI agar (Sigma‐Aldrich, St. Louis, Montana, USA) with 5% defibrinated horse blood and incubated at 37°C in the 5% CO 2 incubator for 24 hr.

Techniques: Standard Deviation

CLSM (×20 magnification) images (0.3 mm 2 ) from within the root canal to illustrate (a) E. faecalis biofilm grown for 10 days and stained using Live/Dead ® viability stain with the green color indicating live cells and the red color showing the dead bacteria (control). (ai) residual biofilm at 3 mm from the canal terminus after syringe irrigation protocol. (b) Passive irrigation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (c) manual‐agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (d) Sonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (e) Ultrasonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus

Journal: MicrobiologyOpen

Article Title: Confocal laser scanning, scanning electron, and transmission electron microscopy investigation of Enterococcus faecalis biofilm degradation using passive and active sodium hypochlorite irrigation within a simulated root canal model

doi: 10.1002/mbo3.455

Figure Lengend Snippet: CLSM (×20 magnification) images (0.3 mm 2 ) from within the root canal to illustrate (a) E. faecalis biofilm grown for 10 days and stained using Live/Dead ® viability stain with the green color indicating live cells and the red color showing the dead bacteria (control). (ai) residual biofilm at 3 mm from the canal terminus after syringe irrigation protocol. (b) Passive irrigation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (c) manual‐agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (d) Sonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (e) Ultrasonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus

Article Snippet: Biofilms were grown from Enterococcus faecalis strain ( ATCC 19433), which was plated onto a BHI agar (Sigma‐Aldrich, St. Louis, Montana, USA) with 5% defibrinated horse blood and incubated at 37°C in the 5% CO 2 incubator for 24 hr.

Techniques: Staining, Bacteria, Control

SEM images (×2,000, ×8,000 magnification) illustrate (a) E. faecalis biofilm grown for 10 days onto the surface of the root canal model (control). (ai) residual biofilm at 3 mm from the canal terminus after syringe irrigation protocol. (b) Passive irrigation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (c) manual‐agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (d) Sonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (e) Ultrasonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus

Journal: MicrobiologyOpen

Article Title: Confocal laser scanning, scanning electron, and transmission electron microscopy investigation of Enterococcus faecalis biofilm degradation using passive and active sodium hypochlorite irrigation within a simulated root canal model

doi: 10.1002/mbo3.455

Figure Lengend Snippet: SEM images (×2,000, ×8,000 magnification) illustrate (a) E. faecalis biofilm grown for 10 days onto the surface of the root canal model (control). (ai) residual biofilm at 3 mm from the canal terminus after syringe irrigation protocol. (b) Passive irrigation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (c) manual‐agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (d) Sonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (e) Ultrasonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus

Article Snippet: Biofilms were grown from Enterococcus faecalis strain ( ATCC 19433), which was plated onto a BHI agar (Sigma‐Aldrich, St. Louis, Montana, USA) with 5% defibrinated horse blood and incubated at 37°C in the 5% CO 2 incubator for 24 hr.

Techniques: Control

TEM (×7,100, 31,000) images illustrate (a) E. faecalis biofilm grown for 10 days onto the surface of the root canal model (control). (ai) residual biofilm at 3 mm from the canal terminus after syringe irrigation protocol. (b) Passive irrigation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (c) manual‐agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (d) Sonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (e) Ultrasonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus

Journal: MicrobiologyOpen

Article Title: Confocal laser scanning, scanning electron, and transmission electron microscopy investigation of Enterococcus faecalis biofilm degradation using passive and active sodium hypochlorite irrigation within a simulated root canal model

doi: 10.1002/mbo3.455

Figure Lengend Snippet: TEM (×7,100, 31,000) images illustrate (a) E. faecalis biofilm grown for 10 days onto the surface of the root canal model (control). (ai) residual biofilm at 3 mm from the canal terminus after syringe irrigation protocol. (b) Passive irrigation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (c) manual‐agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (d) Sonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus. (e) Ultrasonic agitation group; (i) residual biofilm at 2 mm from the canal terminus; (ii) residual biofilm at 1 mm from the canal terminus

Article Snippet: Biofilms were grown from Enterococcus faecalis strain ( ATCC 19433), which was plated onto a BHI agar (Sigma‐Aldrich, St. Louis, Montana, USA) with 5% defibrinated horse blood and incubated at 37°C in the 5% CO 2 incubator for 24 hr.

Techniques: Control

The cell adhesion ability and maximal protein binding capacity of LAB. A monolayer of Int 407 cells (10 4 /well) were mixed without LAB (sample 1), or with 1 × 10 7 CFU of E. faecium (standard strain ATCC 6057) (sample 2), E. faecium 63b-2 (sample 3), or E. faecium 58a-1 (sample 4). After 2 h, the cells were thoroughly washed and fixed with 10% formaldehyde, followed by Gram staining (A). The maximum binding capacity of the AcmA′ fusion protein to LAB was determined as follows. Various concentrations of AcmA′-GFP fusion protein (0, 5, 10, 20, and 50 μg indicated as sample 1–5, respectively) were mixed with 1 × 10 9 CFU of E. faecium 63b-2 at 30 °C for 3 h followed by intensive washes with PBS. After centrifugation, the supernatant containing unbound AcmA-GFP fusion protein was transferred to a new tube and the pellet containing the LAB anchored GFP fusion protein was directly examined by fluorescent microscopy (B). In addition, to evaluate the binding efficiency, the anchored form (C) and free form (D) of GFP fusion proteins were then analyzed with SDS-PAGE. Binding efficiency was determined by the ratio of AcmA′ fusion protein present in the bacteria pellet (anchored form) (C) to that in supernatant (free form) (D).

Journal: Vaccine

Article Title: Avian reovirus sigma C enhances the mucosal and systemic immune responses elicited by antigen-conjugated lactic acid bacteria

doi: 10.1016/j.vaccine.2012.04.043

Figure Lengend Snippet: The cell adhesion ability and maximal protein binding capacity of LAB. A monolayer of Int 407 cells (10 4 /well) were mixed without LAB (sample 1), or with 1 × 10 7 CFU of E. faecium (standard strain ATCC 6057) (sample 2), E. faecium 63b-2 (sample 3), or E. faecium 58a-1 (sample 4). After 2 h, the cells were thoroughly washed and fixed with 10% formaldehyde, followed by Gram staining (A). The maximum binding capacity of the AcmA′ fusion protein to LAB was determined as follows. Various concentrations of AcmA′-GFP fusion protein (0, 5, 10, 20, and 50 μg indicated as sample 1–5, respectively) were mixed with 1 × 10 9 CFU of E. faecium 63b-2 at 30 °C for 3 h followed by intensive washes with PBS. After centrifugation, the supernatant containing unbound AcmA-GFP fusion protein was transferred to a new tube and the pellet containing the LAB anchored GFP fusion protein was directly examined by fluorescent microscopy (B). In addition, to evaluate the binding efficiency, the anchored form (C) and free form (D) of GFP fusion proteins were then analyzed with SDS-PAGE. Binding efficiency was determined by the ratio of AcmA′ fusion protein present in the bacteria pellet (anchored form) (C) to that in supernatant (free form) (D).

Article Snippet: The cell adhesion ability and maximal protein binding capacity of LAB. A monolayer of Int 407 cells (10 4 /well) were mixed without LAB (sample 1), or with 1 × 10 7 CFU of E. faecium (standard strain ATCC 6057) (sample 2), E. faecium 63b-2 (sample 3), or E. faecium 58a-1 (sample 4).

Techniques: Protein Binding, Staining, Binding Assay, Centrifugation, Microscopy, SDS Page, Bacteria

Confirmation of antigen display on LAB by whole-cell ELISA and SDS-PAGE. PBS (sample 1), 20 μg of the purified IBV-S1-AcmA′ (sample 2), or ARV-σC-AcmA′ fusion proteins (sample 3) were incubated with 1 × 10 9 CFU of E. faecium , and then display on the surface of LAB was directly detect by ELISA using anti-His tag antibody (A). Standard deviations are indicated as error bars. For immunization, various fusion proteins (as indicated on the top of gel) were incubated with LAB. After centrifugation, supernatant (unbound, free form of antigenic proteins) and pellet (LAB anchored fusion proteins) were separated and analyzed by SDS-PAGE (B). The binding efficiency was evaluated by the ratio of AcmA′ fusion protein present in the bacteria pellets (anchored form) relative to that in supernatant (free form). The binding assay was done in two duplicates that were then used for intragastric (IG) and intranasal (IN) immunizations (as labeled on the top of gel). M: standard protein size marker (Fermentas).

Journal: Vaccine

Article Title: Avian reovirus sigma C enhances the mucosal and systemic immune responses elicited by antigen-conjugated lactic acid bacteria

doi: 10.1016/j.vaccine.2012.04.043

Figure Lengend Snippet: Confirmation of antigen display on LAB by whole-cell ELISA and SDS-PAGE. PBS (sample 1), 20 μg of the purified IBV-S1-AcmA′ (sample 2), or ARV-σC-AcmA′ fusion proteins (sample 3) were incubated with 1 × 10 9 CFU of E. faecium , and then display on the surface of LAB was directly detect by ELISA using anti-His tag antibody (A). Standard deviations are indicated as error bars. For immunization, various fusion proteins (as indicated on the top of gel) were incubated with LAB. After centrifugation, supernatant (unbound, free form of antigenic proteins) and pellet (LAB anchored fusion proteins) were separated and analyzed by SDS-PAGE (B). The binding efficiency was evaluated by the ratio of AcmA′ fusion protein present in the bacteria pellets (anchored form) relative to that in supernatant (free form). The binding assay was done in two duplicates that were then used for intragastric (IG) and intranasal (IN) immunizations (as labeled on the top of gel). M: standard protein size marker (Fermentas).

Article Snippet: The cell adhesion ability and maximal protein binding capacity of LAB. A monolayer of Int 407 cells (10 4 /well) were mixed without LAB (sample 1), or with 1 × 10 7 CFU of E. faecium (standard strain ATCC 6057) (sample 2), E. faecium 63b-2 (sample 3), or E. faecium 58a-1 (sample 4).

Techniques: Enzyme-linked Immunosorbent Assay, SDS Page, Purification, Incubation, Centrifugation, Binding Assay, Bacteria, Labeling, Marker